Degradation of Synthetic Polypeptides. II. Degradation of Poly-α,L-glutamic Acid by Proteolytic Enzymes in 0.20MSodium Chloride

1964 ◽  
Vol 86 (19) ◽  
pp. 3913-3918 ◽  
Author(s):  
Wilmer G. Miller
Keyword(s):  
Glutamic Acid ◽  
Proteolytic Enzymes ◽  
Synthetic Polypeptides

Controlled release of macromolecules and pharmaceuticals from synthetic polypeptides based on glutamic acid

Biopolymers ◽  
1983 ◽  
Vol 22 (1) ◽  
pp. 547-556 ◽  
Author(s):  
Kenneth R. Sidman ◽  
William D. Steber ◽  
Arthur D. Schwope ◽  
Gayle R. Schnaper
Keyword(s):  
Controlled Release ◽  
Glutamic Acid ◽  
Synthetic Polypeptides

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: VII. A STUDY OF SOME OF THE PROPERTIES OF TWO PROTEASES ISOLATED FROM MORTIERELLA RENISPORA DIXON-STEWART

1954 ◽  
Vol 32 (1) ◽  
pp. 60-67 ◽  
Author(s):  
L. R. Wetter
Keyword(s):  
Enzymatic Activity ◽  
Glutamic Acid ◽  
Culture Medium ◽  
Proteolytic Enzymes ◽  
Isoelectric Points

Two proteases isolated from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) had different isoelectric points but similar pH optimums. The components were inhibited by equal amounts of ovomucoid. Heat studies showed that the constituent moving towards the cathode (cathodic component) was more stable at 58 °C. than the anodic component. The enzyme located in the cathodic component hydrolzyed chloroacetyl-L-tyrosine. The same fraction also hydrolyzed N-carbobenzoxy-α-L-glutamyl-DL-alanine and to a much lesser extent N-carbobenzoxy-α-L-glutamyl-L-glutamic acid. No enzymatic activity could be detected against glycylglycine, diglycylglycine, glycyl-L-proline, seryl-serine, or α-benzoyl-L-argininamide.

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: VII. A STUDY OF SOME OF THE PROPERTIES OF TWO PROTEASES ISOLATED FROM MORTIERELLA RENISPORA DIXON-STEWART

1954 ◽  
Vol 32 (1) ◽  
pp. 60-67 ◽  
Author(s):  
L. R. Wetter
Keyword(s):  
Enzymatic Activity ◽  
Glutamic Acid ◽  
Culture Medium ◽  
Proteolytic Enzymes ◽  
Isoelectric Points

Two proteases isolated from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) had different isoelectric points but similar pH optimums. The components were inhibited by equal amounts of ovomucoid. Heat studies showed that the constituent moving towards the cathode (cathodic component) was more stable at 58 °C. than the anodic component. The enzyme located in the cathodic component hydrolzyed chloroacetyl-L-tyrosine. The same fraction also hydrolyzed N-carbobenzoxy-α-L-glutamyl-DL-alanine and to a much lesser extent N-carbobenzoxy-α-L-glutamyl-L-glutamic acid. No enzymatic activity could be detected against glycylglycine, diglycylglycine, glycyl-L-proline, seryl-serine, or α-benzoyl-L-argininamide.

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: V. EXTRACELLULAR PEPTIDASES PRODUCED BY FUNGI GROWN IN SUBMERGED CULTURE

1953 ◽  
Vol 31 (8) ◽  
pp. 697-704 ◽  
Author(s):  
W. B. McConnell ◽  
E. Y. Spencer ◽  
J. A. Trew
Keyword(s):  
Activation Energy ◽  
Glutamic Acid ◽  
Submerged Culture ◽  
Culture Media ◽  
Proteolytic Enzymes ◽  
Gliocladium Roseum ◽  
Rapid Hydrolysis ◽  
Hydrolysis Of ◽  
Extracellular Peptidases ◽  
Dipeptidase Activity

The culture media from selected fungi grown in submerged culture have been shown to contain enzymes capable of hydrolyzing some synthetic dipeptides and their derivatives. Readily measurable amounts of aminopeptidase, carboxypeptidase, and dipeptidase activity were found, and differences between the systems elaborated by different organisms were observed. The most rapid hydrolysis of N-cbzo-α-L-glutamyl-L-glutamic acid (I) and of N-cbzo-α-L-glutamyl-DL-alanine (II) by Gliocladium roseum PRL 86 occurred at pH 4.8 to 4.9. I was hydrolyzed most rapidly by Alternariatenuis PRL 369 at pH 4.7. The activation energies for the hydrolysis of I by PRL 369 and of II by PRL 86 were found to be 11,000 and 15,000 calories per mole, respectively. The activation energy for the hydrolysis of I by PRL 86 was estimated as being between 10,000 and 13,000 calories per mole.

scholarly journals N-Heterocyclic Carbene-Catalyzed Random Copolymerization of N-Carboxyanhydrides of α-Amino Acids

Polymers ◽  
2021 ◽  
Vol 13 (21) ◽  
pp. 3674
Author(s):  
Kuen Hee Eom ◽  
Seokhyeon Baek ◽  
Il Kim
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Primary Structure ◽  
Reactivity Ratio ◽  
Synthetic Polypeptides ◽  
Random Placement ◽  
Natural Peptides ◽  
The Relationship ◽  
Method Show

Synthetic polypeptides prepared from N-carboxyanhydrides (NCAs) of α-amino acids are useful for elucidating the relationship between the primary structure of natural peptides and their immunogenicity. In this study, complex copolypeptide sequences were prepared using a recently developed technique; specifically, the random copolymerization of l-alanine NCA with NCAs of l-glutamic acid 5-benzylester (Bn-Glu NCA), S-benzyl-cysteine (Bn-Cys NCA), O-benzyl-l-serine (Bn-Ser NCA), and l-phenylalanine (Phe NCA) was performed using N-heterocyclic carbene (NHC) catalysts. The NHC-initiated Ala NCA/Bn-Glu NCA and Ala NCA/Bn-Cys NCA copolymerization reactions achieved 90% conversion within 30 min. The reactivity ratio values estimated using the Kelen and Tüdos method show that poly(Bn-Glu-co-Ala) and poly(Bn-Cys-co-Ala) have random repeating units with rich alternating sequences, whereas poly(Bn-Ser-co-Ala) and poly(Phe-co-Ala) contain a larger proportion of Ala-repeating units than Bn-Ser and Phe in random placement.

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